3.

3
Cells use simple carbohydrates (sugars) for energy and to build other molecules. Monosaccharides
(simple sugars) are bonded together to form disaccharides (two sugars), oligosaccharides (a few sugars),
and polysaccharides (many sugars). Cellulose, starch, and glycogen are polysaccharides that consist of
the same glucose monomers, bonded different ways. Chitin is a polysaccharide of nitrogen-containing
sugar monomers.

3.4
Lipids in biological systems are partially or entirely nonpolar. A fatty acid is a lipid with a carboxyl group
head and a long hydrocarbon tail. Fatty acids have a dual chemical character: the carboxyl group is
hydrophilic, and the hydrocarbon tail is hydrophobic. Only single bonds link the carbons in the tail of a
saturated fatty acid; the tail of an unsaturated fatty acid has one or more double bonds.

Fats are triglycerides, which have three fatty acid tails bonded to a glycerol head. Triglycerides are
entirely hydrophobic. A saturated fat has no double bonds in its fatty acid tails (all three are saturated).
By contrast, an unsaturated fat has one or more unsaturated fatty acid tails. A monounsaturated fat has
one double bond among its three fatty acid tails; a polyunsaturated fat has two or more.

The basic structure of cell membranes is the lipid bilayer, which consists mainly of phospholipids.

Steroids, with four carbon rings and no fatty acid tails, serve important physiological roles such as
starting materials for sex hormone synthesis.

Waxes are water-repellent substances that consist of complex, varying mixtures of lipids.

3.5
Peptides and polypeptides are (short and long) chains of amino acids linked by peptide bonds. A protein
consists of one or more polypeptides. The order of amino acids making up a polypeptide (primary
structure) dictates the type of protein and its shape.

A protein’s shape is the source of its function. Each type of protein has a unique primary structure, but
almost all proteins have similar patterns of secondary structure—helices, sheets, loops, and turns—that
form as the polypeptide lengthens and hydrogen bonds form between its amino acids.

Helices, sheets, loops, and turns of a lengthening polypeptide fold into functional domains (tertiary
structure). Many proteins, including most enzymes, consist of two or more polypeptides (quaternary
structure). Fibrous proteins aggregate into much larger structures.

A protein that can bind to lipids is a lipoprotein; a protein with attached oligosaccharides is a
glycoprotein.

Changes in a protein’s structure may alter its function. Hydrogen bonds that stabilize protein shape may
be disrupted by shifts in pH or temperature, or exposure to detergent or some salts. This causes
denaturation, which means the protein loses its shape, and so loses its function. Prion diseases are a
fatal consequence of misfolded proteins.